Research workbench
PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 9.00 coordinates)
Analyse PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B2G
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (insulin a chain); Protein (insulin B chain)
- UniProt
- P01315
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (insulin a chain) | protein | 21 | 48% helix, 5% strand | P01315 |
| B | Protein (insulin B chain) | protein | 30 | 47% helix, 3% strand | P01315 |
Interfaces
1 interface between chains.
- A–B · 799 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1B2G · PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 9.00… · the same entry in another collection · chain A against A, TM-score 1.00
- P01315 · AlphaFold monomer V2.0 prediction for insulin (P01315) · a predicted model of the same protein · chain B against A, TM-score 0.38
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01315
- Elsewhere: RCSB PDB 1B2G · PDBe 1B2G · UniProt P01315
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